Engineering amyloid and amyloid-like morphologies of β-lactoglobulin

Hoppenreijs, Loes J.G.; Fitzner, Laura; Ruhmlieb, T.; Heyn, Timon R.; Schild, K.; Goot, Atze Jan van der; Boom, R.M.; Steffen‐Heins, Anja; Schwarz, Karin; Keppler, Julia K.

doi:10.1016/j.foodhyd.2021.107301

Cited by 29 publications

(12 citation statements)

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“…ANFs formed by heating a β-lactoglobulin protein solution at 90 °C and pH 2 exhibited the generic morphology of semiflexible amyloid nanofibrils . According to AFM images, ANFs had a high aspect ratio of approximately 1070 (average length of 4.9 μm and diameter of 4.5 nm) (Figure S2).…”

Section: Resultsmentioning

confidence: 99%

“…ANFs formed by heating a β-lactoglobulin protein solution at 90 °C and pH 2 exhibited the generic morphology of semiflexible amyloid nanofibrils. 21 According to AFM images, ANFs had a high aspect ratio of approximately 1070 (average length of 4.9 μm and diameter of 4.5 nm) ( Figure S2 ). The high aspect ratio enables the fibrils to form self-supporting physically entangled networks at low concentrations, which are a desired characteristic for forming robust aerogels.…”

Section: Resultsmentioning

confidence: 99%

“…β-Lactoglobulin can be obtained from whey, which is cheap and highly available as a byproduct of the cheese-making process in the dairy industry . Under controlled conditions, β-lactoglobulin can form long, multistranded, semiflexible ANFs with remarkable structural stability and mechanical properties due to their rigid cross-β sheet core structure. , As a result of their high aspect ratio, these long and slender ANFs are capable of forming stable gel networks at low solid contents, and the gel-to-solid transition of such a gel system can be used for making multifunctional amyloid-based aerogels. Although the potential of aerogels from ANF in the remediation of environmental pollutants has been shown in different studies, − the material preparation most frequently requires time- and energy-demanding drying processes (such as freeze-drying or supercritical drying) to prevent shrinkage, cracking, and collapse of the ANF-based aerogels during fabrication.…”

Section: Introductionmentioning

confidence: 99%

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Green Ambient-Dried Aerogels with a Facile pH-Tunable Surface Charge for Adsorption of Cationic and Anionic Contaminants with High Selectivity

et al. 2022

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The fabrication of reusable, sustainable adsorbents from low-cost, renewable resources via energy efficient methods is challenging. This paper presents wet-stable, carboxymethylated cellulose nanofibril (CNF) and amyloid nanofibril (ANF) based aerogel-like adsorbents prepared through efficient and green processes for the removal of metal ions and dyes from water. The aerogels exhibit tunable densities (18–28 kg m–3), wet resilience, and an interconnected porous structure (99% porosity), with a pH controllable surface charge for adsorption of both cationic (methylene blue and Pb(II)) and anionic (brilliant blue, congo red, and Cr(VI)) model contaminants. The Langmuir saturation adsorption capacity of the aerogel was calculated to be 68, 79, and 42 mg g–1 for brilliant blue, Pb(II), and Cr(VI), respectively. Adsorption kinetic studies for the adsorption of brilliant blue as a model contaminant demonstrated that a pseudo-second-order model best fitted the experimental data and that an intraparticle diffusion model suggests that there are three adsorption stages in the adsorption of brilliant blue on the aerogel. Following three cycles of adsorption and regeneration, the aerogels maintained nearly 97 and 96% of their adsorption capacity for methylene blue and Pb(II) as cationic contaminants and 89 and 80% for brilliant blue and Cr(VI) as anionic contaminants. Moreover, the aerogels showed remarkable selectivity for Pb(II) in the presence of calcium and magnesium as background ions, with a selectivity coefficient more than 2 orders of magnitude higher than calcium and magnesium. Overall, the energy-efficient and sustainable fabrication procedure, along with good structural stability, reusability, and selectivity, makes these aerogels very promising for water purification applications.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Green Ambient-Dried Aerogels with a Facile pH-Tunable Surface Charge for Adsorption of Cationic and Anionic Contaminants with High Selectivity

et al. 2022

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“…At present, this poses an increasing challenge to many companies producing protein pharmaceuticals, because aggregates of therapeutic proteins can induce immune responses that render them useless and potentially even dangerous for pharmaceutical purposes [ 10 ]. Moreover, controlled self-assembly can also be a critical step in peptide drug formulation [ 11 ] or materials production [ 12 , 13 , 14 ].…”

Section: Introductionmentioning

confidence: 99%

Influence of Centrifugation and Shaking on the Self-Assembly of Lysozyme Fibrils

et al. 2022

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Protein self-assembly into fibrils and oligomers plays a key role in the etiology of degenerative diseases. Several pathways for this self-assembly process have been described and shown to result in different types and ratios of final assemblies, therewith defining the effective physiological response. Known factors that influence assembly pathways are chemical conditions and the presence or lack of agitation. However, in natural and industrial systems, proteins are exposed to a sequence of different and often complex mass transfers. In this paper, we compare the effect of two fundamentally different mass transfer processes on the fibrilization process. Aggregation-prone solutions of hen egg white lysozyme were subjected to predominantly non-advective mass transfer by employing centrifugation and to advective mass transport represented by orbital shaking. In both cases, fibrilization was triggered, while in quiescent only oligomers were formed. The fibrils obtained by shaking compared to fibrils obtained through centrifugation were shorter, thicker, and more rigid. They had rod-like protofibrils as building blocks and a significantly higher β-sheet content was observed. In contrast, fibrils from centrifugation were more flexible and braided. They consisted of intertwined filaments and had low β-sheet content at the expense of random coil. To the best of our knowledge, this is the first evidence of a fibrilization pathway selectivity, with the fibrilization route determined by the mass transfer and mixing configuration (shaking versus centrifugation). This selectivity can be potentially employed for directed protein fibrilization.

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“…Such cross-links may be involved in amyloid formation (Li et al 2013 ); however, they are not a prerequisite (Mossuto et al 2011 ). A growing view on amyloids is that it is a common structural property of proteins (Hoppenreijs et al 2021 ), specially globular proteins (Guijarro et al 1998 ), and under optimum conditions most proteins can form amyloid structures. The non-covalent interactions, predominantly hydrophobic interactions and hydrogen bonding, are credited for β-sheet stacking forming an ordered structure (Schleeger et al 2013 ).…”

Section: Resultsmentioning

confidence: 99%

Ultrasound-induced protein restructuring and ordered aggregation to form amyloid crystals

et al. 2022

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Amyloid crystals, a form of ordered protein aggregates documented relatively recently, have not been studied as extensively as amyloid fibres. This study investigates the formation of amyloid crystals with low frequency ultrasound (20 kHz) using β-lactoglobulin, as a model protein for amyloid synthesis. Acoustic cavitation generates localised zones of intense shear, with extreme heat and pressure that could potentially drive the formation of amyloid structures at ambient bulk fluid temperatures (20 ± 1 °C). Thioflavin T fluorescence and electron microscopy showed that low-frequency ultrasound at 20 W/cm3 input power induced β-stacking to produce amyloid crystals in the mesoscopic size range, with a mean length of approximately 22 µm. FTIR spectroscopy indicated a shift towards increased intermolecular antiparallel β-sheet content. An increase in sonication time (0–60 min) and input power (4–24 W/cm3) increased the mean crystal length, but this increase was not linearly proportional to sonication time and input power due to the delayed onset of crystal growth. We propose that acoustic cavitation causes protein unfolding and aggregation and imparts energy to aggregates to cross the torsion barrier, to achieve their lowest energy state as amyloid crystals. The study contributes to a further understanding of protein chemistry relating to the energy landscape of folding and aggregation. Ultrasound presents opportunities for practical applications of amyloid structures, presenting a more adaptable and scalable approach for synthesis. Graphical abstract

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Engineering amyloid and amyloid-like morphologies of β-lactoglobulin

Cited by 29 publications

References 123 publications

Green Ambient-Dried Aerogels with a Facile pH-Tunable Surface Charge for Adsorption of Cationic and Anionic Contaminants with High Selectivity

Green Ambient-Dried Aerogels with a Facile pH-Tunable Surface Charge for Adsorption of Cationic and Anionic Contaminants with High Selectivity

Influence of Centrifugation and Shaking on the Self-Assembly of Lysozyme Fibrils

Ultrasound-induced protein restructuring and ordered aggregation to form amyloid crystals

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